Background: Irisin, which corresponds to the FNDC5 receptor ectodomain, is a purported exercise-induced myokine produced by cleavage. Results: Irisin forms an extensive intersubunit ␤-sheet dimer with an FNIII-like fold. Conclusion: Irisin forms a continuous ␤-sheet dimer not observed previously for any FNIII protein and may be representative of a new FNIII class. Significance: The preformed irisin dimer suggests mechanisms for ligand and receptor activation.

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Enterohemorrhagic Escherichia coli (EHEC) is a foodborne pathogen causing hemorrhagic colitis and hemolytic uremic syndrome. EHEC colonizes the intestinal tract through a range of virulence factors encoded by the locus of enterocyte effacement (LEE), as well as Shiga toxin. Although the factors involved in colonization and disease are well characterized, how EHEC regulates its expression in response to a host encounter is not well understood. Here, we report that EHEC perceives attachment to host cells as a mechanical cue that leads to expression of LEE-encoded virulence genes. This signal is transduced via the LEE-encoded global regulator of LEEencoded regulator (Ler) and global regulator of Ler and is further enhanced by levels of shear force similar to peristaltic forces in the intestinal tract. Our data suggest that, in addition to a range of chemical environmental signals, EHEC is capable of sensing and responding to mechanical cues to adapt to its host's physiology.enterohemorrhagic Escherichia coli | locus of enterocyte effacement | attaching/effacing pathogens | gastrointestinal infection | mechanosensing

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